Evangelia Pantazaka1, Evangelia Papadimitriou2. 1. Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras GR26504, Greece. 2. Laboratory of Molecular Pharmacology, Department of Pharmacy, University of Patras GR26504, Greece. Electronic address: epapad@upatras.gr.
Abstract
BACKGROUND: Glycosylation is a multi-step post-translational enzymatic process which enhances the functional diversity of secreted or membrane proteins and is implicated in physiological and pathological conditions. Chondroitin sulfate (CS) chains are glycosaminoglycan chains, consisting of disaccharide units of glucuronic acid and N-acetylgalactosamine, attached to proteins as part of proteoglycans. SCOPE OF REVIEW: The existing knowledge on glycosylation by CS (CS glycanation) of cell membrane proteins and receptors, such as syndecans, chondroitin sulfate proteoglycan 4, betaglycan, neuropilin-1, integrins and receptor protein tyrosine phosphatase β/ζ, is summarized and the importance of CS glycanation in growth factor-induced migration, angiogenesis and tumor growth and invasion is described. MAJOR CONCLUSIONS: Identification of glycosylation so far used to be a means of further characterizing and categorizing proteins and receptors. Although there is a significant amount of information regarding the interaction of growth factors with CS chains, very little information exists on the core proteins involved. It is now evident that there is more than meets the eye regarding the addition of glycans. GENERAL SIGNIFICANCE: Future effort should focus on characterizing CS glycanation of membrane proteins and receptors of interest in an attempt to elucidate its contribution in fine-tuning growth factor-induced signaling. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties.
BACKGROUND: Glycosylation is a multi-step post-translational enzymatic process which enhances the functional diversity of secreted or membrane proteins and is implicated in physiological and pathological conditions. Chondroitin sulfate (CS) chains are glycosaminoglycan chains, consisting of disaccharide units of glucuronic acid and N-acetylgalactosamine, attached to proteins as part of proteoglycans. SCOPE OF REVIEW: The existing knowledge on glycosylation by CS (CS glycanation) of cell membrane proteins and receptors, such as syndecans, chondroitin sulfateproteoglycan 4, betaglycan, neuropilin-1, integrins and receptor protein tyrosine phosphatase β/ζ, is summarized and the importance of CS glycanation in growth factor-induced migration, angiogenesis and tumor growth and invasion is described. MAJOR CONCLUSIONS: Identification of glycosylation so far used to be a means of further characterizing and categorizing proteins and receptors. Although there is a significant amount of information regarding the interaction of growth factors with CS chains, very little information exists on the core proteins involved. It is now evident that there is more than meets the eye regarding the addition of glycans. GENERAL SIGNIFICANCE: Future effort should focus on characterizing CS glycanation of membrane proteins and receptors of interest in an attempt to elucidate its contribution in fine-tuning growth factor-induced signaling. This article is part of a Special Issue entitled Matrix-mediated cell behaviour and properties.
Authors: Rebeca Kawahara; Daniela C Granato; Carolina M Carnielli; Nilva K Cervigne; Carine E Oliveria; César Rivera; César A R Martinez; Sami Yokoo; Felipe P Fonseca; Marcio Lopes; Alan R Santos-Silva; Edgard Graner; Ricardo D Coletta; Adriana Franco Paes Leme Journal: PLoS One Date: 2014-12-15 Impact factor: 3.240
Authors: A Agrawal; M J Khan; D E Graugnard; M Vailati-Riboni; S L Rodriguez-Zas; J S Osorio; J J Loor Journal: Bioinform Biol Insights Date: 2017-04-28